Expression of Extracellular Matrix Proteins in Ovarian Serous Tumors

Salani, Ritu; Neuberger, Ilana; Kurman, Robert J.; Bristow, Robert E.; Chang, Hsueh-Wei; Wang, Tian Li; Shih, Ie Ming

doi:10.1097/01.pgp.0000229994.02815.f9

Cited by 33 publications

(21 citation statements)

References 16 publications

(4 reference statements)

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“…This would be expected of an ECM protein. In addition, a number of proteomic and microarray studies of human tissues (Table 1) have identified EMILIN2 in extracellular fluids (plasma, synovial, amniotic and seminal plasma), stem cells (hematopoietic, mesenchymal, osteoblasts), stimulated endometrial stromal cells, cancer cells (hepatic, lymphocytic leukemia, colorectal cancer, and ovarian cancer), and as a cell surface marker for human embryonic stem cell-derived cardiomyocytes [36-50]. A recent study [40] reported down-regulation of EMILIN2 in brain arteriovenous malformations.…”

Section: Discussionmentioning

confidence: 99%

EMILIN2 (Elastin microfibril interface located protein), potential modifier of thrombosis

Hoover‐Plow

2011

Thrombosis Journal

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BackgroundElastin microfibril interface located protein 2 (EMILIN2) is an extracellular glycoprotein associated with cardiovascular development. While other EMILIN proteins are reported to play a role in elastogenesis and coagulation, little is known about EMILIN2 function in the cardiovascular system. The objective of this study was to determine whether EMILIN2 could play a role in thrombosis.ResultsEMILIN2 mRNA was expressed in 8 wk old C57BL/6J mice in lung, heart, aorta and bone marrow, with the highest expression in bone marrow. In mouse cells, EMILIN2 mRNA expression in macrophages was higher than expression in endothelial cells and fibroblasts. EMILIN2 was identified with cells and extracellular matrix by immunohistochemistry in the carotid and aorta. After carotid ferric chloride injury, EMILIN2 was abundantly expressed in the thrombus and inhibition of EMILIN2 increased platelet de-aggregation after ADP-stimulated platelet aggregation.ConclusionsThese results suggest EMILIN2 could play a role in thrombosis as a constituent of the vessel wall and/or a component of the thrombus.

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Section: Discussionmentioning

confidence: 99%

EMILIN2 (Elastin microfibril interface located protein), potential modifier of thrombosis

Hoover‐Plow

2011

Thrombosis Journal

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“…Tumor cells are known to interfere with the normal programming of ECM biosynthesis and can extensively modify the structure and composition of the matrix [6]. Alterations in the extracellular environment are critical for tumor initiation and progression and intra-peritoneal dissemination [7][8][9][10][11][12][13][14][15][16].…”

Section: Introductionmentioning

confidence: 99%

Versican induces a pro-metastatic ovarian cancer cell behavior which can be inhibited by small hyaluronan oligosaccharides

Ween

Hummitzsch

Rodgers

et al. 2010

Clin Exp Metastasis

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The assembly of pericellular matrix containing hyaluronan (HA) and versican has been shown to be a pre-requisite for proliferation and migration of mesenchymal cells. In this study, we investigated whether treatment with recombinant versican could induce the formation of a pericellular matrix by ovarian cancer cells (OVCAR-3, OVCAR-5, and SKOV-3) and promote their motility, invasion, and adhesion to peritoneal cells in vitro. We also determined whether versican-induced pericellular matrix formation and metastatic cancer cell behavior could be blocked by small HA oligosaccharides. Only combined treatment with recombinant versican and HA resulted in pericellular matrix formation by OVCAR-5 and SKOV-3 but not by OVCAR-3 cells, which lack the HA receptor, CD44. The motility of OVCAR-5 and SKOV-3 cells was significantly increased in scratch wound and chemotaxis assays following treatment with recombinant versican and HA. Versican and HA also promoted invasion of SKOV-3 and OVCAR-5 cells but had no effect on OVCAR-3 cells. We have demonstrated that exogenous HA significantly increased OVCAR-5 and SKOV-3 adhesion to peritoneal cells but adhesion was not further increased by versican treatment. Small HA oligomers (6-10 disaccharides) were able to significantly block formation of pericellular matrix by OVCAR-5 cells, as well as the increased motility and invasion induced by recombinant versican. HA oligomers also significantly blocked OVCAR-5 adhesion to peritoneal cells both in the presence and absence of exogenous HA. The dependence of CD44 for the versican and HA mediated effects were demonstrated by the inhibition of pericellular matrix formation as well as motility and invasion of OVCAR-5 cells following treatment with CD44 neutralizing antibody in the presence of versican and HA. We conclude that the acquisition of a HA/versican pericellular matrix by ovarian cancer cells increases their metastatic potential. HA oligomers can block this mechanism and are promising inhibitors of ovarian cancer dissemination.

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“…This hypothesis seems not to be supported by two different studies of gene expression and proteomic analysis related to matrix protein profiles in ovarian carcinomas and soft tissue osteosarcomas where EMILIN1 was upregulated [142,143]. A pro-or anti-tumor action could be exerted by EMILIN1 in a tissue-specific manner.…”

Section: Emilin1 and Cancermentioning

confidence: 90%

A Rare Bird among Major Extracellular Matrix Proteins: EMILIN1 and the Tumor Suppressor Function

Colombatti¹

2013

J Carcinog Mutagen

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Extracellular Matrix (ECM) proteins constitute a complex network of macromolecules with distinctive physical, biochemical, and biomechanical properties. They are expressed dynamically and their cellular functions are highly dependent upon cues from the local environment. ECM proteins primarily by interaction with integrins on the cell surface initiate downstream signaling events that involve diverse cellular functions. Although tightly controlled under normal development, the ECM is commonly deregulated and becomes disorganized in diseases such as cancer. Abnormal ECM affects cancer progression by directly promoting cellular transformation, metastasis and facilitates tumor-associated angiogenesis and inflammation, and thus leads to generation of a tumorigenic microenvironment. In this review, we summarize and discuss the current knowledge of the diverse promoting or inhibiting role played by selected members (collagen, fibronectin, tenascin, thrombospondin, LTBP-2, fibulin, CCN1, decorin, EMILIN2) of the ECM play within the microenvironment that influences tumor progression with an emphasis on EMILIN1. This glycoprotein, a member of the gC1q domain superfamily, is involved in the maintenance of the blood pressure, the proper function of lymphatic capillaries and collecting vessels and, via the interaction with the α4β1 and/or the α9β1 integrins, regulates cell proliferation. This last function highlights the peculiar role of EMILIN1 as an anti-proliferative member of the ECM and likely a novel tumor suppressor.

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Expression of Extracellular Matrix Proteins in Ovarian Serous Tumors

Cited by 33 publications

References 16 publications

EMILIN2 (Elastin microfibril interface located protein), potential modifier of thrombosis

EMILIN2 (Elastin microfibril interface located protein), potential modifier of thrombosis

Versican induces a pro-metastatic ovarian cancer cell behavior which can be inhibited by small hyaluronan oligosaccharides

A Rare Bird among Major Extracellular Matrix Proteins: EMILIN1 and the Tumor Suppressor Function

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